Literature summary for 2.4.1.18 extracted from

Ban, X.; Li, C.; Zhang, Y.; Gu, Z.; Cheng, L.; Hong, Y.; Li, Z.
Importance of C-terminal extension in thermophilic 1,4-alpha-glucan branching enzyme from Geobacillus thermoglucosidans STB02 (2020), Appl. Biochem. Biotechnol., 190, 1010-1022 .

Search for more literature for 2.4.1.18

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Parageobacillus thermoglucosidasius

General Stability

General Stability	Organism
truncation of the C-terminal extension results in greater stability and solubility than the wild type, as well as a lower sensitivity to the presence of added metal ions	Parageobacillus thermoglucosidasius

Inhibitors

Inhibitors	Comment	Organism	Structure
Al3+	the wild type enzyme shows bout 75% residual activity at 10 mM. The C-terminally truncated enzyme shows about 95% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Ca2+	the wild type enzyme shows about 90% residual activity at 10 mM. The C-terminally truncated enzyme shows about 97% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Co2+	the wild type enzyme shows complete inhibition at 3 mM. The C-terminally truncated enzyme shows about 28% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Cr2+	the wild type enzyme shows about 75% residual activity at 10 mM. The C-terminally truncated enzyme shows about 94% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Cu2+	the wild type enzyme shows about 10% residual activity at 10 mM. The C-terminally truncated enzyme shows about 51% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Fe2+	the wild type enzyme shows about 85% residual activity at 10 mM. The C-terminally truncated enzyme shows about 97% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Fe3+	the wild type enzyme shows about 78% residual activity at 10 mM. The C-terminally truncated enzyme shows about 95% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Mn2+	the wild type enzyme shows about 35% residual activity at 10 mM. The C-terminally truncated enzyme shows about 69% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Ni2+	the wild type enzyme shows about 2% residual activity at 10 mM. The C-terminally truncated enzyme shows about 25% residual activity at 10 mM	Parageobacillus thermoglucosidasius
Zn2+	the wild type enzyme shows about 18% residual activity at 10 mM. The C-terminally truncated enzyme shows about 58% residual activity at 10 mM	Parageobacillus thermoglucosidasius

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ba2+	the wild type enzyme shows 100% activity at 1 mM. The C-terminally truncated enzyme shows about 102% activity at 1 mM	Parageobacillus thermoglucosidasius
Ca2+	the C-terminally truncated enzyme shows about 105% activity at 1 mM	Parageobacillus thermoglucosidasius
K+	the wild type enzyme shows about 128% activity at 1 mM. The C-terminally truncated enzyme shows about 103% activity at 1 mM	Parageobacillus thermoglucosidasius
Mg2+	the wild type and C-terminally truncated enzyme show 100% activity at 1 mM	Parageobacillus thermoglucosidasius
Na+	the wild type enzyme shows about 118% activity at 1 mM. The C-terminally truncated enzyme shows about 106% activity at 1 mM	Parageobacillus thermoglucosidasius

Organism

Organism	UniProt	Comment	Textmining
Parageobacillus thermoglucosidasius	A0A068F9H3	-	-
Parageobacillus thermoglucosidasius STB02	A0A068F9H3	-	-

Purification (Commentary)

Purification (Comment)	Organism
HiTrap ANX column chromatography and HiTrap phenyl column chromatography	Parageobacillus thermoglucosidasius

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
amylopectin	-	Parageobacillus thermoglucosidasius	?	-	?
amylopectin	-	Parageobacillus thermoglucosidasius STB02	?	-	?
amylose	-	Parageobacillus thermoglucosidasius	?	-	?
amylose	-	Parageobacillus thermoglucosidasius STB02	?	-	?

Synonyms

Synonyms	Comment	Organism
GBE	-	Parageobacillus thermoglucosidasius

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Release 2023.1 (January 2023)